Determination of meso-.ALPHA.,.EPSILON.-diaminopimelate with meso-.ALPHA.,.EPSILON.-diaminopimelate D-dehydrogenase.
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چکیده
منابع مشابه
Properties of meso - a , € - Diaminopimelate D - Dehydrogenase from Bacillus sphaericus
meso-a,eDiaminopimelate D-dehydrogenase, which has been purified to homogeneity from the extract of Bacillus sphaericus IF0 3626, has a molecular weight of about 80,000 and consists of two subunits identical in molecular weight (approximately 40,000). The enzyme has a high substrate specificity. In addition to mso-a,diaminopimelate, lanthionine is deaminated by the enzyme to a far lesser extent...
متن کاملAnalogs of diaminopimelic acid as inhibitors of meso-diaminopimelate dehydrogenase and LL-diaminopimelate epimerase.
Analogs 1-8 of diaminopimelic acid (DAP) were synthesized and tested for inhibition of purified meso-DAP D-dehydrogenase from Bacillus sphaericus and of LL-DAP epimerase from Escherichia coli. The dehydrogenase was assayed by monitoring NADPH formation spectrophotometrically at 340 nm. N-Hydroxy DAP 4, N-amino DAP 5, and 4-methylene DAP 6 are substrates of the dehydrogenase with relative rates ...
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Species-specific antimicrobial therapy has the potential to combat the increasing threat of antibiotic resistance and alteration of the human microbiome. We therefore set out to demonstrate the beginning of a pathogen-selective drug discovery method using the periodontal pathogen Porphyromonas gingivalis as a model. Through our knowledge of metabolic networks and essential genes we identified a...
متن کاملStructural insight into the thermostable NADP(+)-dependent meso-diaminopimelate dehydrogenase from Ureibacillus thermosphaericus.
Crystal structures of the thermostable meso-diaminopimelate dehydrogenase (DAPDH) from Ureibacillus thermosphaericus were determined for the enzyme in the apo form and in complex with NADP(+) and N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid. The main-chain coordinates of the enzyme showed notable similarity to those of Symbiobacterium thermophilum DAPDH. However, the subunit arrangeme...
متن کاملCrystal structure of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-diaminopimelate ligase from Escherichia coli.
UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:meso-diaminopimelate ligase is a cytoplasmic enzyme that catalyzes the addition of meso-diaminopimelic acid to nucleotide precursor UDP-N-acetylmuramoyl-l-alanyl-d-glutamate in the biosynthesis of bacterial cell-wall peptidoglycan. The crystal structure of the Escherichia coli enzyme in the presence of the final product of the enzymatic reaction, UDP-Mu...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1980
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.44.2125